Sequence of LON_ECOLI
EC Number:3.4.21.53
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
hydrolysis of proteins in presence of ATP
Other sequences found for EC No. 3.4.21.53
General information:
Sequence
0 MNPERSERIE IPVLPLRDVV VYPHMVIPLF VGREKSIRCL EAAMDHDKKI MLVAQKEAST
60 DEPGVNDLFT VGTVASILQM LKLPDGTVKV LVEGLQRARI SALSDNGEHF SAKAEYLESP
120 TIDEREQEVL VRTAISQFEG YIKLNKKIPP EVLTSLNSID DPARLADTIA AHMPLKLADK
180 QSVLEMSDVN ERLEYLMAMM ESEIDLLQVE KRIRNRVKKQ MEKSQREYYL NEQMKAIQKE
240 LGEMDDAPDE NEALKRKIDA AKMPKEAKEK AEAELQKLKM MSPMSAEATV VRGYIDWMVQ
300 VPWNARSKVK KDLRQAQEIL DTDHYGLERV KDRILEYLAV QSRVNKIKGP ILCLVGPPGV
360 GKTSLGQSIA KATGRKYVRM ALGGVRDEAE IRGHRRTYIG SMPGKLIQKM AKVGVKNPLF
420 LLDEIDKMSS DMRGDPASAL LEVLDPEQNV AFSDHYLEVD YDLSDVMFVA TSNSMNIPAP
480 LLDRMEVIRL SGYTEDEKLN IAKRHLLPKQ IERNALKKGE LTVDDSAIIG IIRYYTREAG
540 VRGLEREISK LCRKAVKQLL LDKSLKHIEI NGDNLHDYLG VQRFDYGRAD NENRVGQVTG
600 LAWTEVGGDL LTIETACVPG KGKLTYTGSL GEVMQESIQA ALTVVRARAE KLGINPDFYE
660 KRDIHVHVPE GATPKDGPSA GIAMCTALVS CLTGNPVRAD VAMTGEITLR GQVLPIGGLK
720 EKLLAAHRGG IKTVLIPFEN KRDLEEIPDN VIADLDIHPV KRIEEVLTLA LQNEPSGMQV
780 VTAK
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
54577
Thomas C.D.,Modha J.,Razzaq T.M.,Cullis P.M.,Rivett A.
Controlled high-level expression of the lon gene of Escherichia coli allows overproduction of Lon protease.
Gene
136
237-242
1993
54578
Amerik A.Y.,Chistyakova L.G.,Ostroumova N.I.,Gurevich A.I.,Antonov V.K.
Cloning, expression and structure of the functionally active shortened lon gene in Escherichia coli.
Bioorg. Khim.
14
408-411
1988
54579
Amerik A.I.U.,Antonov V.K.,Ostroumova N.I.,Rotanova T.V.,Chistiakova L.G.
Cloning, structure and expression of the full-size lon gene in Escherichia coli coding for ATP-dependent La-proteinase.
Bioorg. Khim.
16
869-880
1990
54580
Fischer H.,Glockshuber R.
ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coli.
J. Biol. Chem.
268
22502-22507
1993
54581
Chin D.T.,Goff S.A.,Webster T.,Smith T.,Goldberg A.L.
Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La.
J. Biol. Chem.
263
11718-11728
1988
54583
Blattner F.R.,Plunkett G. III,Bloch C.A.,Perna N.T.,Burland V.,Riley M.,Collado-Vides J.,Glasner J.D.,Rode C.K.,Mayhew G.F.,Gregor J.,Davis N.W.,Kirkpatrick H.A.,Goeden M.A.,Rose D.J.,Mau B.,Shao Y.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
54584
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
54585
Gayda R.C.,Stephens P.E.,Hewick R.,Schoemaker J.M.,Dreyer W.J.,Markovitz A.
Regulatory region of the heat shock-inducible capR (lon) gene: DNA and protein sequences.
J. Bacteriol.
162
271-275
1985
54586
Fu G.K.,Smith M.J.,Markovitz D.M.
Bacterial protease Lon is a site-specific DNA-binding protein.
J. Biol. Chem.
272
534-538
1997
54587
Fischer H.,Glockshuber R.
A point mutation within the ATP-binding site inactivates both catalytic functions of the ATP-dependent protease La (Lon) from Escherichia coli.
FEBS Lett.
356
101-103
1994
54588
Van Melderen L.,Bernard P.,Couturier M.
Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria.
Mol. Microbiol.
11
1151-1157
1994
54589
VanBogelen R.A.,Abshire K.Z.,Moldover B.,Olson E.R.,Neidhardt F.C.
Escherichia coli proteome analysis using the gene-protein database.
Electrophoresis
18
1243-1251
1997
54590
Starkova N.N.,Koroleva E.P.,Rumsh L.D.,Ginodman L.M.,Rotanova T.V.
Mutations in the proteolytic domain of Escherichia coli protease Lon impair the ATPase activity of the enzyme.
FEBS Lett.
422
218-220
1998
54591
Gonzalez M.,Frank E.G.,Levine A.S.,Woodgate R.
Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis.
Genes Dev.
12
3889-3899
1998
54592
Ebel W.,Skinner M.M.,Dierksen K.P.,Scott J.M.,Trempy J.E.
A conserved domain in Escherichia coli Lon protease is involved in substrate discriminator activity.
J. Bacteriol.
181
2236-2243
1999
54593
Thomas-Wohlever J.,Lee I.
Kinetic characterization of the peptidase activity of Escherichia coli Lon reveals the mechanistic similarities in ATP-dependent hydrolysis of peptide and protein substrates.
Biochemistry
41
9418-9425
2002
54594
Besche H.,Zwickl P.
The Thermoplasma acidophilum Lon protease has a Ser-Lys dyad active site.
Eur. J. Biochem.
271
4361-4365
2004
54595
Christensen S.K.,Maenhaut-Michel G.,Mine N.,Gottesman S.,Gerdes K.,Van Melderen L.
Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system.
Mol. Microbiol.
51
1705-1717
2004
54596
Vineyard D.,Patterson-Ward J.,Lee I.
Single-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon protease.
Biochemistry
45
4602-4610
2006
54597
Shah I.M.,Wolf R.E. Jr.
Sequence requirements for Lon-dependent degradation of the Escherichia coli transcription activator SoxS: identification of the SoxS residues critical to proteolysis and specific inhibition of in vitro degradation by a peptide comprised of the N-terminal 21 amino acid residues.
J. Mol. Biol.
357
718-731
2006
54598
Park S.C.,Jia B.,Yang J.K.,Van D.L.,Shao Y.G.,Han S.W.,Jeon Y.J.,Chung C.H.,Cheong G.W.
Oligomeric structure of the ATP-dependent protease La (Lon) of Escherichia coli.
Mol. Cells
21
129-134
2006
54599
Duval V.,Nicoloff H.,Levy S.B.
Combined inactivation of lon and ycgE decreases multidrug susceptibility by reducing the amount of OmpF porin in Escherichia coli.
Antimicrob. Agents Chemother.
53
4944-4948
2009
54600
Maisonneuve E.,Shakespeare L.J.,Joergensen M.G.,Gerdes K.
Bacterial persistence by RNA endonucleases.
Proc. Natl. Acad. Sci. U.S.A.
108
13206-13211
2011
54601
Maisonneuve E.,Shakespeare L.J.,Joergensen M.G.,Gerdes K.
Proc. Natl. Acad. Sci. U.S.A.
115
0-0
2018
54602
Hansen S.,Vulic M.,Min J.,Yen T.J.,Schumacher M.A.,Brennan R.G.,Lewis K.
Regulation of the Escherichia coli HipBA toxin-antitoxin system by proteolysis.
PLoS ONE
7
0-0
2012
54603
Tripathi A.,Dewan P.C.,Siddique S.A.,Varadarajan R.
MazF-induced growth inhibition and persister generation in Escherichia coli.
J. Biol. Chem.
289
4191-4205
2014
54604
Botos I.,Melnikov E.E.,Cherry S.,Tropea J.E.,Khalatova A.G.,Rasulova F.,Dauter Z.,Maurizi M.R.,Rotanova T.V.,Wlodawer A.,Gustchina A.
The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site.
J. Biol. Chem.
279
8140-8148
2004
54605
Botos I.,Melnikov E.E.,Cherry S.,Khalatova A.G.,Rasulova F.S.,Tropea J.E.,Maurizi M.R.,Rotanova T.V.,Gustchina A.,Wlodawer A.
Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution.
J. Struct. Biol.
146
113-122
2004
54606
Li M.,Rasulova F.,Melnikov E.E.,Rotanova T.V.,Gustchina A.,Maurizi M.R.,Wlodawer A.
Crystal structure of the N-terminal domain of E. coli Lon protease.
Protein Sci.
14
2895-2900
2005
